Design and Early Experience With a Real-World Surgical Registry.

OBJECTIVES: We describe the rationale, design, and methods and 6-year experience with a real-world surgical registry for female pelvic reconstructive and incontinence procedures and postoperative outcomes. METHODS: The primary goal of creating this registry was to establish the feasibility of prospective data capture for all urogynecologic procedures. Data captured included baseline demographics, surgical procedures, perioperative complications, and subjective and objective findings up to 36 months after surgery. RESULTS: The Pelvic Reconstruction and Incontinence Surgery ± Mesh Registry was developed over 3 years to include 194 unique variables for prospective data capture. The registry was implemented in December 2010, and data from 924 separate case events from a single surgeon were recorded, comprising 100% surgical case capture. Cases included a variety of procedures representing a comprehensive urogynecology practice on 804 unique patients. Patients who were asked to participate in long-term follow-up (n = 299) returned with attendance of 96% at 6 weeks, 64% at 6 months, 51% at 12 months, 39% at 24 months, and 22% at 36 months. CONCLUSIONS: The Pelvic Reconstruction and Incontinence Surgery ± Mesh Registry effectively captured all urogynecologic procedures for the purpose of quality improvement. This real-world tool demonstrates that 100% case capture is feasible and provides valuable information for the highly motivated surgeon, although adequate long-term follow-up is limited. Additional research is needed to better understand the role of surgical registries for quality improvement and development of patient-centered strategies to increase long-term follow-up.

A retained secretory signal peptide mediates high density lipoprotein (HDL) assembly and function of haptoglobin-related protein.

Haptoglobin-related protein (Hpr) is a component of a minor subspecies of high density lipoproteins (HDL) that function in innate immunity. Here we show that assembly of Hpr into HDL is mediated by its retained N-terminal signal peptide, an unusual feature for a secreted protein and the major difference between Hpr and the soluble acute phase protein haptoglobin (Hp). The 18-amino acid signal peptide is necessary for binding to HDL and interacts directly with the hydrocarbon region of lipids. Utilizing model liposomes, we show that the rate of assembly and steady-state distribution of Hpr in lipid particles is mediated by the physical property of lipid fluidity. Dye release assays reveal that Hpr interacts more rapidly with fluid liposomes. Conversely, steady-state binding assays indicate that more rigid lipid compositions stabilize Hpr association. Lipid association also plays a role in facilitating hemoglobin binding by Hpr. Our data may offer an explanation for the distinct distribution of Hpr among HDL subspecies. Rather than protein-protein interactions mediating localization, direct interaction with phospholipids and sensitivity to lipid fluidity may be sufficient for localization of Hpr and may represent a mechanism of HDL subspeciation.